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Targeting of Vacuolar Membrane Localized Members of the TPK Channel Family 被引量:5

Targeting of Vacuolar Membrane Localized Members of the TPK Channel Family
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摘要 Four members of the tandem-pore potassium channel family of Arabidopsis thaliana (TPK1, 2, 3, and 5) reside in the vacuolar membrane, whereas TPK4 is a plasma membrane K^+-channel. By constructing chimeras between TPK1 and TPK4, we attempted to identify channel domains involved in the trafficking process and found that the TPK1 cytoplasmic C-terminal domain (CT) is critical for the ERas well as Golgi-sorting steps. Following site-directed mutagenesis, we identified a diacidic motif (DLE) required for ER-export of TPK1. However, this diacidic motif in the C-terminus is not conserved among other members of the TPK family, and TPK3 sorting is independent of its CT. Moreover, the 14-3-3 binding site of TPK1, essential for channel activation, is not involved in channel sorting. Four members of the tandem-pore potassium channel family of Arabidopsis thaliana (TPK1, 2, 3, and 5) reside in the vacuolar membrane, whereas TPK4 is a plasma membrane K^+-channel. By constructing chimeras between TPK1 and TPK4, we attempted to identify channel domains involved in the trafficking process and found that the TPK1 cytoplasmic C-terminal domain (CT) is critical for the ERas well as Golgi-sorting steps. Following site-directed mutagenesis, we identified a diacidic motif (DLE) required for ER-export of TPK1. However, this diacidic motif in the C-terminus is not conserved among other members of the TPK family, and TPK3 sorting is independent of its CT. Moreover, the 14-3-3 binding site of TPK1, essential for channel activation, is not involved in channel sorting.
出处 《Molecular Plant》 SCIE CAS CSCD 北大核心 2008年第6期938-949,共12页 分子植物(英文版)
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